Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria
12 páginas, 6 figuras
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Language: | English |
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Oxford University Press
2021
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Subjects: | Chloroplast Thioredoxins, Thioredoxin-Disulfide Reductase, Peroxiredoxins, |
Online Access: | http://hdl.handle.net/10261/245541 http://dx.doi.org/10.13039/501100003329 |
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dig-irnasa-es-10261-2455412021-12-28T16:51:53Z Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria Martínez Buey, Rubén Fernández-Justel, David González Holgado, Gloria Martínez-Júlvez, Marta González-López, Adrián Velázquez-Campoy, Adrián Medina, Milagros Buchanan, Bob B. Balsera, Mónica Ministerio de Ciencia, Innovación y Universidades (España) Ministerio de Economía y Competitividad (España) Balsera, Mónica [0000-0002-5586-6050] Chloroplast Thioredoxins Thioredoxin-Disulfide Reductase Peroxiredoxins 12 páginas, 6 figuras Thioredoxin reductases control the redox state of thioredoxins (Trxs)—ubiquitous proteins that regulate a spectrum of enzymes by dithiol–disulfide exchange reactions. In most organisms, Trx is reduced by NADPH via a thioredoxin reductase flavoenzyme (NTR), but in oxygenic photosynthetic organisms, this function can also be performed by an iron-sulfur ferredoxin (Fdx)-dependent thioredoxin reductase (FTR) that links light to metabolic regulation. We have recently found that some cyanobacteria, such as the thylakoid-less Gloeobacter and the ocean-dwelling green oxyphotobacterium Prochlorococcus, lack NTR and FTR but contain a thioredoxin reductase flavoenzyme (formerly tentatively called deeplyrooted thioredoxin reductase or DTR), whose electron donor remained undefined. Here, we demonstrate that Fdx functions in this capacity and report the crystallographic structure of the transient complex between the plant-type Fdx1 and the thioredoxin reductase flavoenzyme from Gloeobacter violaceus. Thereby, our data demonstrate that this cyanobacterial enzyme belongs to the Fdx flavin-thioredoxin reductase (FFTR) family, originally described in the anaerobic bacterium Clostridium pasteurianum. Accordingly, the enzyme hitherto termed DTR is renamed FFTR. Our experiments further show that the redox-sensitive peptide CP12 is modulated in vitro by the FFTR/Trx system, demonstrating that FFTR functionally substitutes for FTR in light-linked enzyme regulation in Gloeobacter. Altogether, we demonstrate the FFTR is spread within the cyanobacteria phylum and propose that, by substituting for FTR, it connects the reduction of target proteins to photosynthesis. Besides, the results indicate that FFTR acquisition constitutes a mechanism of evolutionary adaptation in marine phytoplankton such as Prochlorococcus that live in low-iron environments. This work was supported by the Spanish Ministry of Science and Innovation—State Research Agency (MICINN) Grants [PID2019-110900GB-I00 to M.B., PID2019-109671GB-I00 to R.M.B., BFU-2016-78232-P to A.V.-C., and PID2019-103901GB-I00 to M.M.], and the Government of Aragón FEDER [Grupo de Referencia Biología Estructural (E35_20R to M.M., and E45_17R to A.V.-C.)]. D.F.J. was supported by a predoctoral contract from the Junta de Castilla y León. A.G.- L. acknowledges support from CSIC Jae-Intro program. Peer reviewed 2021-07-09T06:54:10Z 2021-07-09T06:54:10Z 2021 artículo http://purl.org/coar/resource_type/c_6501 Plant Physiology 186: 285-296 (2021) 0032-0889 http://hdl.handle.net/10261/245541 10.1093/plphys/kiab072 1532-2548 http://dx.doi.org/10.13039/501100003329 33599267 en #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# #PLACEHOLDER_PARENT_METADATA_VALUE# info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-110900GB-I00 info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-109671GB-I00 info:eu-repo/grantAgreement/MINECO/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU-2016-78232-P tMICIU/ICTI2017-2020/PID2019-103901GB-I00 Publisher's version http://dx.doi.org/10.1093/plphys/kiab072 Sí open Oxford University Press |
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Chloroplast Thioredoxins Thioredoxin-Disulfide Reductase Peroxiredoxins Chloroplast Thioredoxins Thioredoxin-Disulfide Reductase Peroxiredoxins |
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Chloroplast Thioredoxins Thioredoxin-Disulfide Reductase Peroxiredoxins Chloroplast Thioredoxins Thioredoxin-Disulfide Reductase Peroxiredoxins Martínez Buey, Rubén Fernández-Justel, David González Holgado, Gloria Martínez-Júlvez, Marta González-López, Adrián Velázquez-Campoy, Adrián Medina, Milagros Buchanan, Bob B. Balsera, Mónica Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria |
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12 páginas, 6 figuras |
author2 |
Ministerio de Ciencia, Innovación y Universidades (España) |
author_facet |
Ministerio de Ciencia, Innovación y Universidades (España) Martínez Buey, Rubén Fernández-Justel, David González Holgado, Gloria Martínez-Júlvez, Marta González-López, Adrián Velázquez-Campoy, Adrián Medina, Milagros Buchanan, Bob B. Balsera, Mónica |
format |
artículo |
topic_facet |
Chloroplast Thioredoxins Thioredoxin-Disulfide Reductase Peroxiredoxins |
author |
Martínez Buey, Rubén Fernández-Justel, David González Holgado, Gloria Martínez-Júlvez, Marta González-López, Adrián Velázquez-Campoy, Adrián Medina, Milagros Buchanan, Bob B. Balsera, Mónica |
author_sort |
Martínez Buey, Rubén |
title |
Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria |
title_short |
Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria |
title_full |
Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria |
title_fullStr |
Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria |
title_full_unstemmed |
Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria |
title_sort |
unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria |
publisher |
Oxford University Press |
publishDate |
2021 |
url |
http://hdl.handle.net/10261/245541 http://dx.doi.org/10.13039/501100003329 |
work_keys_str_mv |
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1777665406022975488 |